Structure of a GH51 α- L -arabinofuranosidase from Meripilus giganteus : conserved substrate recognition from bacteria to fungi

DOI: 10.1107/S205979832001253X

Authors: Nicholas G. S. Mcgregor (The University of York) , Johan P. Turkenburg (University of York) , Kristian B. R. Mørkeberg Krogh (Novozymes A/S) , Jens Erik Nielsen (Novozymes A/S) , Marta Artola (Leiden University) , Keith A. Stubbs (The University of Western Australia) , Herman S. Overkleeft (Leiden University) , Gideon J. Davies (The University of York)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section D Structural Biology , VOL 76

State: Published (Approved)
Published: November 2020
Diamond Proposal Number(s): 18598

Abstract: α-L-Arabinofuranosidases from glycoside hydrolase family 51 use a stereochemically retaining hydrolytic mechanism to liberate nonreducing terminal α-L-arabinofuranose residues from plant polysaccharides such as arabinoxylan and arabinan. To date, more than ten fungal GH51 α-L-arabinofuranosidases have been functionally characterized, yet no structure of a fungal GH51 enzyme has been solved. In contrast, seven bacterial GH51 enzyme structures, with low sequence similarity to the fungal GH51 enzymes, have been determined. Here, the crystallization and structural characterization of MgGH51, an industrially relevant GH51 α-L-arabinofuranosidase cloned from Meripilus giganteus, are reported. Three crystal forms were grown in different crystallization conditions. The unliganded structure was solved using sulfur SAD data collected from a single crystal using the I23 in vacuo diffraction beamline at Diamond Light Source. Crystal soaks with arabinose, 1,4-dideoxy-1,4-imino-L-arabinitol and two cyclophellitol-derived arabinose mimics reveal a conserved catalytic site and conformational itinerary between fungal and bacterial GH51 α-L-arabino­furanosidases.

Journal Keywords: glycoside hydrolases; arabinofuranosidases; cyclophellitol; iminosugar; sulfur SAD

Diamond Keywords: Bacteria; Fungi; Enzymes

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography , I23-Long wavelength MX

Added On: 20/10/2020 13:46

Documents:
dw5211.pdf

Discipline Tags:

Catalysis Life Sciences & Biotech Structural biology Chemistry Biochemistry

Technical Tags:

Diffraction Macromolecular Crystallography (MX)